Publication | Open Access
Microsecond and nanosecond polyproline II helix formation in aqueous nanodrops measured by mass spectrometry
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Citations
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References
2016
Year
EngineeringPeptide EngineeringSuper-hydrophobic SurfacePeptide ScienceChemistryAnalytical UltracentrifugationProtein FoldingNs Time ConstantsAqueous NanodropsMolecular SimulationMacromolecular AssembliesPolymer ChemistryBiophysicsNanotechnologyResidue PeptidesMolecular ModelingStructural BiologyBiomolecular EngineeringMacromolecular SciencePolymer ScienceMass SpectrometryPeptide SynthesisMolecular BiophysicsMedicine
The 1.5 μs and <400 ns time constants for the formation of polyproline II helix structures in 21 and 16 residue peptides, respectively, are measured using rapid mixing from theta-glass emitters coupled with mass spectrometry. Results from these studies should serve as useful benchmarks for comparison with computational simulation results.
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